Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial

Gene

IDH3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+2 Publications, Mn2+1 PublicationNote: Divalent metal cations; Mn2+ or Mg2+. Activity higher in presence of Mn2+ than of Mg2+. Binds 1 Mg2+ or Mn2+ ion per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits can be allosterically activated by citrate (CIT) or/and ADP, and the two activators can act independently or synergistically. The heterodimer composed of IDH3A and IDH3B subunits cannot be allosterically regulated and the allosteric regulation of the heterotetramer is through the IDH3G subunit and not the IDH3B subunit. The IDH3G subunit contains the allosteric site which consists of a CIT-binding site and an ADP-binding site, and the binding of CIT and ADP causes conformational changes at the allosteric site which are transmitted to the active site in the catalytic subunit (IDH3A) through a cascade of conformational changes at the heterodimer interface, leading to stabilization of the isocitrate-binding at the active site and thus activation of the enzyme. ATP can activate the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits at low concentrations but inhibits their activities at high concentrations, whereas ATP exhibits only inhibitory effect on the heterodimer composed of IDH3A and IDH3B subunits.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 26.7 sec(-1) for the heterotetramer with isocitrate as substrate. kcat is 14.6 sec(-1) for the heterodimer composed of IDH3A and IDH3B subunits with isocitrate as substrate. kcat is 9.72 sec(-1) for the heterodimer composed of IDH3A and IDH3G subunits with isocitrate as substrate. kcat is 23.4 sec(-1) for the heterotetramer with isocitrate as substrate in the presence of citrate and ATP. kcat is 11.9 sec(-1) for the heterodimer composed of IDH3A and IDH3G subunits with isocitrate as substrate in the presence of citrate and ATP. kcat is 28.4 sec(-1) for the heterotetramer with isocitrate as substrate in the presence of citrate and ADP. kcat is 15.8 sec(-1) for the heterodimer composed of IDH3A and IDH3B subunits with isocitrate as substrate in the presence of citrate and ADP. kcat is 17.6 sec(-1) for the heterodimer composed of IDH3A and IDH3G subunits with isocitrate as substrate in the presence of citrate and ADP.1 Publication
    1. Vmax=20.0 µmol/min/mg enzyme with isocitrate as substrate (heterotetramer)1 Publication
    2. Vmax=10.9 µmol/min/mg enzyme with isocitrate as substrate (heterodimer composed of IDH3A and IDH3B subunits)1 Publication
    3. Vmax=7.29 µmol/min/mg enzyme with isocitrate as substrate (heterodimer composed of IDH3A and IDH3G subunits)1 Publication
    4. Vmax=20.7 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate (heterotetramer)1 Publication
    5. Vmax=11.2 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate (heterodimer composed of IDH3A and IDH3B subunits)1 Publication
    6. Vmax=10.0 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate (heterodimer composed of IDH3A and IDH3G subunits)1 Publication
    7. Vmax=22.1 µmol/min/mg enzyme with isocitrate as substrate in the presence of ADP (heterotetramer)1 Publication
    8. Vmax=11.2 µmol/min/mg enzyme with isocitrate as substrate in the presence of ADP (heterodimer composed of IDH3A and IDH3B subunits)1 Publication
    9. Vmax=9.42 µmol/min/mg enzyme with isocitrate as substrate in the presence of ADP (heterodimer composed of IDH3A and IDH3G subunits)1 Publication
    10. Vmax=21.3 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate and ADP (heterotetramer)1 Publication
    11. Vmax=11.9 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate and ADP (heterodimer composed of IDH3A and IDH3B subunits)1 Publication
    12. Vmax=13.1 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate and ADP (heterodimer composed of IDH3A and IDH3G subunits)1 Publication
    13. Vmax=17.7 µmol/min/mg enzyme with isocitrate as substrate in the presence of ATP (heterotetramer)1 Publication
    14. Vmax=6.62 µmol/min/mg enzyme with isocitrate as substrate in the presence ATP (heterodimer composed of IDH3A and IDH3G subunits)1 Publication
    15. Vmax=17.6 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate and ATP (heterotetramer)1 Publication
    16. Vmax=8.94 µmol/min/mg enzyme with isocitrate as substrate in the presence of citrate and ATP (heterodimer composed of IDH3A and IDH3G subunits)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei115Substrate1 Publication1
    Binding sitei125Substrate1 Publication1
    Binding sitei146Substrate1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei153Critical for catalysis2 Publications1
    Sitei200Critical for catalysis1 Publication1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi233Magnesium or manganese1 Publication1
    Metal bindingi257Magnesium or manganese1 Publication1
    Metal bindingi261Magnesium or manganese1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • isocitrate dehydrogenase (NAD+) activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • NAD binding Source: InterPro

    GO - Biological processi

    • carbohydrate metabolic process Source: ProtInc
    • tricarboxylic acid cycle Source: UniProtKB-KW

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processTricarboxylic acid cycle
    LigandMagnesium, Manganese, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:ENSG00000166411-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-71403 Citric acid cycle (TCA cycle)

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P50213

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC:1.1.1.412 Publications)
    Alternative name(s):
    Isocitric dehydrogenase subunit alpha
    NAD(+)-specific ICDH subunit alpha
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:IDH3A
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000166411.13

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:5384 IDH3A

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    601149 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P50213

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Mitochondrion

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi152E → A: No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. 1 Publication1
    Mutagenesisi153Y → F: Complete loss of activity of the heterotetramer, heterodimer composed of IDH3A and IDH3B subunits and the heterodimer composed of IDH3A and IDH3G subunits with no effect on their oligomeric states. 1 Publication1
    Mutagenesisi169K → A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. 1 Publication1
    Mutagenesisi200K → A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. 1 Publication1
    Mutagenesisi202N → A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate. 1 Publication1
    Mutagenesisi208D → A: Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. 1 Publication1
    Mutagenesisi255Y → A: Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    3419

    Open Targets

    More...
    OpenTargetsi
    ENSG00000166411

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA29632

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB00157 NADH

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    IDH3A

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    1708399

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 27MitochondrionCombined sourcesAdd BLAST27
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001443628 – 366Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrialAdd BLAST339

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei77N6-succinyllysineBy similarity1
    Modified residuei101PhosphothreonineBy similarity1
    Modified residuei223N6-acetyllysineBy similarity1
    Modified residuei343N6-acetyllysine; alternateCombined sources1
    Modified residuei343N6-succinyllysine; alternateBy similarity1
    Modified residuei350N6-succinyllysineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P50213

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P50213

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P50213

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P50213

    PeptideAtlas

    More...
    PeptideAtlasi
    P50213

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P50213

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    56201
    56202 [P50213-2]

    2D gel databases

    USC-OGP 2-DE database

    More...
    OGPi
    P50213

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00030702

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P50213

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P50213

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P50213

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P50213

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000166411 Expressed in 231 organ(s), highest expression level in heart

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_IDH3A

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P50213 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P50213 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA041465
    HPA062971

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer containing one IDH3A and one IDH3B subunit and the heterodimer containing one IDH3A and one IDH3G subunit assemble into a heterotetramer (which contains two subunits of IDH3A, one of IDH3B and one of IDH3G) and further into the heterooctamer.2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    109645, 55 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-553 Mitochondrial isocitrate dehydrogenase complex (NAD+)

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P50213

    Protein interaction database and analysis system

    More...
    IntActi
    P50213, 16 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000299518

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1366
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5GREX-ray2.65A28-366[»]
    5GRFX-ray2.50A28-366[»]
    5GRHX-ray2.80A28-366[»]
    5GRIX-ray2.31A28-366[»]
    5GRLX-ray2.79A28-366[»]
    5YVTX-ray2.40A28-366[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P50213

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P50213

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0785 Eukaryota
    COG0473 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000153381

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000021113

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG052080

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P50213

    KEGG Orthology (KO)

    More...
    KOi
    K00030

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HGTAPKH

    Database of Orthologous Groups

    More...
    OrthoDBi
    868374at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P50213

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105692

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR019818 IsoCit/isopropylmalate_DH_CS
    IPR004434 Isocitrate_DH_NAD
    IPR024084 IsoPropMal-DH-like_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00180 Iso_dh, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01329 Iso_dh, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00175 mito_nad_idh, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00470 IDH_IMDH, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P50213-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MAGPAWISKV SRLLGAFHNP KQVTRGFTGG VQTVTLIPGD GIGPEISAAV
    60 70 80 90 100
    MKIFDAAKAP IQWEERNVTA IQGPGGKWMI PSEAKESMDK NKMGLKGPLK
    110 120 130 140 150
    TPIAAGHPSM NLLLRKTFDL YANVRPCVSI EGYKTPYTDV NIVTIRENTE
    160 170 180 190 200
    GEYSGIEHVI VDGVVQSIKL ITEGASKRIA EFAFEYARNN HRSNVTAVHK
    210 220 230 240 250
    ANIMRMSDGL FLQKCREVAE SCKDIKFNEM YLDTVCLNMV QDPSQFDVLV
    260 270 280 290 300
    MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD
    310 320 330 340 350
    MANPTALLLS AVMMLRHMGL FDHAARIEAA CFATIKDGKS LTKDLGGNAK
    360
    CSDFTEEICR RVKDLD
    Length:366
    Mass (Da):39,592
    Last modified:October 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i695F6A34F97430CF
    GO
    Isoform 2 (identifier: P50213-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-78: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:288
    Mass (Da):31,381
    Checksum:iBF8327BD4AA7D3EC
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    H0YL72H0YL72_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    331Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YLI6H0YLI6_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    134Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YKD0H0YKD0_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    109Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YNF5H0YNF5_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    87Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YMU3H0YMU3_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    175Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YM46H0YM46_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    48Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YNF8H0YNF8_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    60Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YMY5H0YMY5_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    45Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    Q68D72Q68D72_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A DKFZp686A08194
    37Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H0YM64H0YM64_HUMAN
    Isocitrate dehydrogenase [NAD] subu...
    IDH3A
    46Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    There are more potential isoformsShow all

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0145161 – 78Missing in isoform 2. 1 PublicationAdd BLAST78

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U07681 mRNA Translation: AAA85639.1
    AL442090 mRNA Translation: CAC09449.1
    CH471136 Genomic DNA Translation: EAW99181.1
    CH471136 Genomic DNA Translation: EAW99182.1
    BC021967 mRNA Translation: AAH21967.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS10297.1 [P50213-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S55282

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_005521.1, NM_005530.2 [P50213-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.591110

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000299518; ENSP00000299518; ENSG00000166411 [P50213-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3419

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:3419

    UCSC genome browser

    More...
    UCSCi
    uc002bdd.4 human [P50213-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U07681 mRNA Translation: AAA85639.1
    AL442090 mRNA Translation: CAC09449.1
    CH471136 Genomic DNA Translation: EAW99181.1
    CH471136 Genomic DNA Translation: EAW99182.1
    BC021967 mRNA Translation: AAH21967.1
    CCDSiCCDS10297.1 [P50213-1]
    PIRiS55282
    RefSeqiNP_005521.1, NM_005530.2 [P50213-1]
    UniGeneiHs.591110

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5GREX-ray2.65A28-366[»]
    5GRFX-ray2.50A28-366[»]
    5GRHX-ray2.80A28-366[»]
    5GRIX-ray2.31A28-366[»]
    5GRLX-ray2.79A28-366[»]
    5YVTX-ray2.40A28-366[»]
    ProteinModelPortaliP50213
    SMRiP50213
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109645, 55 interactors
    ComplexPortaliCPX-553 Mitochondrial isocitrate dehydrogenase complex (NAD+)
    CORUMiP50213
    IntActiP50213, 16 interactors
    STRINGi9606.ENSP00000299518

    Chemistry databases

    DrugBankiDB00157 NADH

    PTM databases

    CarbonylDBiP50213
    iPTMnetiP50213
    PhosphoSitePlusiP50213
    SwissPalmiP50213

    Polymorphism and mutation databases

    BioMutaiIDH3A
    DMDMi1708399

    2D gel databases

    OGPiP50213
    REPRODUCTION-2DPAGEiIPI00030702

    Proteomic databases

    EPDiP50213
    jPOSTiP50213
    MaxQBiP50213
    PaxDbiP50213
    PeptideAtlasiP50213
    PRIDEiP50213
    ProteomicsDBi56201
    56202 [P50213-2]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    3419
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000299518; ENSP00000299518; ENSG00000166411 [P50213-1]
    GeneIDi3419
    KEGGihsa:3419
    UCSCiuc002bdd.4 human [P50213-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    3419
    DisGeNETi3419
    EuPathDBiHostDB:ENSG00000166411.13

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    IDH3A
    HGNCiHGNC:5384 IDH3A
    HPAiHPA041465
    HPA062971
    MIMi601149 gene
    neXtProtiNX_P50213
    OpenTargetsiENSG00000166411
    PharmGKBiPA29632

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0785 Eukaryota
    COG0473 LUCA
    GeneTreeiENSGT00940000153381
    HOGENOMiHOG000021113
    HOVERGENiHBG052080
    InParanoidiP50213
    KOiK00030
    OMAiHGTAPKH
    OrthoDBi868374at2759
    PhylomeDBiP50213
    TreeFamiTF105692

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000166411-MONOMER
    ReactomeiR-HSA-71403 Citric acid cycle (TCA cycle)
    SABIO-RKiP50213

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    IDH3A human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    IDH3A

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    3419

    Protein Ontology

    More...
    PROi
    PR:P50213

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000166411 Expressed in 231 organ(s), highest expression level in heart
    CleanExiHS_IDH3A
    ExpressionAtlasiP50213 baseline and differential
    GenevisibleiP50213 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR019818 IsoCit/isopropylmalate_DH_CS
    IPR004434 Isocitrate_DH_NAD
    IPR024084 IsoPropMal-DH-like_dom
    PfamiView protein in Pfam
    PF00180 Iso_dh, 1 hit
    SMARTiView protein in SMART
    SM01329 Iso_dh, 1 hit
    TIGRFAMsiTIGR00175 mito_nad_idh, 1 hit
    PROSITEiView protein in PROSITE
    PS00470 IDH_IMDH, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIDH3A_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P50213
    Secondary accession number(s): D3DW83, Q9H3X0
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: January 16, 2019
    This is version 188 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again